<oai_dc:dc xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:oai_dc="http://www.openarchives.org/OAI/2.0/oai_dc/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/oai_dc/ http://www.openarchives.org/OAI/2.0/oai_dc.xsd">
  <dc:creator>Casalou, Cristina</dc:creator>
  <dc:creator>Faustino, Alexandra</dc:creator>
  <dc:creator>Silva, Fernanda</dc:creator>
  <dc:creator>Ferreira, Inês C.</dc:creator>
  <dc:creator>Vaqueirinho, Daniela</dc:creator>
  <dc:creator>Ferreira, Andreia</dc:creator>
  <dc:creator>Castanheira, Pedro</dc:creator>
  <dc:creator>Barona, Teresa</dc:creator>
  <dc:creator>Ramalho, José S.</dc:creator>
  <dc:creator>Serpa, Jacinta</dc:creator>
  <dc:creator>Félix, Ana</dc:creator>
  <dc:creator>Barral, Duarte C.</dc:creator>
  <dc:date>2019-09-29</dc:date>
  <dc:description xmlns:ns0="xml" ns0:lang="en">Breast cancer is the first cause of cancer-related mortality among women worldwide, according to the most recent  estimates. This mortality is mainly caused by the tumors’ ability to form metastases. Cancer cell migration and  invasion are essential for metastasis and rely on the interplay between actin cytoskeleton remodeling and cell  adhesion. Therefore, understanding the mechanisms by which cancer cell invasion is controlled may provide new  strategies to impair cancer progression. We investigated the role of the ADP-ribosylation factor (Arf)-like (Arl)  protein Arl13b in breast cancer cell migration and invasion in vitro, using breast cancer cell lines and in vivo, using  mouse orthotopic models. We show that Arl13b silencing inhibits breast cancer cell migration and invasion in vitro,  as well as cancer progression in vivo. We also observed that Arl13b is upregulated in breast cancer cell lines and  patient tissue samples. Moreover, we found that Arl13b localizes to focal adhesions (FAs) and interacts with β3- integrin. Upon Arl13b silencing, β3-integrin cell surface levels and FA size are increased and integrin-mediated  signaling is inhibited. Therefore, we uncover a role for Arl13b in breast cancer cell migration and invasion and  provide a new mechanism for how ARL13B can function as an oncogene, through the modulation of integrin- mediated signaling.</dc:description>
  <dc:format>application/pdf</dc:format>
  <dc:identifier>https://susi.usi.ch/global/documents/319139</dc:identifier>
  <dc:identifier>https://n2t.net/ark:/12658/srd1319139</dc:identifier>
  <dc:identifier>https://susi.usi.ch/documents/319139/files/Casalou_C_2019.pdf</dc:identifier>
  <dc:language>eng</dc:language>
  <dc:relation>info:eu-repo/semantics/altIdentifier/doi/10.3390/cancers11101461</dc:relation>
  <dc:relation>info:eu-repo/semantics/altIdentifier/ark/12658/srd1319139</dc:relation>
  <dc:rights>info:eu-repo/semantics/openAccess</dc:rights>
  <dc:rights>CC BY</dc:rights>
  <dc:source>Cancers. - 2019, vol. 11, no. 10, p. 1461</dc:source>
  <dc:subject xmlns:ns1="xml" ns1:lang="en">Integrins</dc:subject>
  <dc:subject xmlns:ns2="xml" ns2:lang="en">Actin cytoskeleton</dc:subject>
  <dc:subject xmlns:ns3="xml" ns3:lang="en">Cancer progression</dc:subject>
  <dc:subject xmlns:ns4="xml" ns4:lang="en">Arl proteins</dc:subject>
  <dc:subject xmlns:ns5="xml" ns5:lang="en">Cell-extracellular matrix adhesion</dc:subject>
  <dc:subject>info:eu-repo/classification/udc/61</dc:subject>
  <dc:title xmlns:ns6="xml" ns6:lang="en">Arl13b regulates breast cancer cell migration and invasion by controlling integrin-mediated signaling</dc:title>
  <dc:type>http://purl.org/coar/resource_type/c_6501</dc:type>
</oai_dc:dc>